Amyloid precursor protein

Amyloid precursor protein (APP) is thought to regulate transcription. For detailed discussion see Human APP and Human APP Intracellular Domain Complex with Fe65-PTB2.

3D structures of amyloid precursor protein
3nyj – hAPP E2 domain – human 3ktm – hAPP residues 18-190 1z0q, 2beg – hAPP β-peptide – NMR 1ze7, 2bp4 – hAPP zinc-binding domain – NMR 2fjz, 2fma - hAPP residues 133-189 1owt - hAPP residues 133-189]] - NMR 1rw6 - hAPP residues 346-551 1tkn - hAPP residues 460-569 - NMR 1qyt, 1qwp, 1qxc - hAPP residues 25-35 – NMR

Amyloid precursor protein binary complex

1ze9 - hAPP zinc-binding domain + Zn – NMR 2fk1, 2fk2, 2fk3, 2fkl - hAPP residues 133-189 + Cu 3jti, 3gci – hAPP peptide + phospholipase A2 3l81 - hAPP peptide + AP-4 complex subunit μ-1 3ifl, 3ifn, 3ifo, 3ifp, 2r0w - hAPP peptide + antibody 2wk3 - hAPP residues 1-42 + insulin degrading enzyme 3dxc - hAPP residues 739-770 + Fe65-PTB2 3dxd, 3dxe - hAPP residues 739-770 (mutant) + Fe65-PTB2<BR /> 2roz - hAPP peptide + Fe65 C terminal<BR /> 2otk - hAPP residues 672-711 + ZAB3 affibody dimer - NMR<BR />